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Translocation. A. Colicin E3-cleaved (closed circles) or control (open circles) pre-translocation complexes (0.1 μM) were mixed in a quench-flow apparatus with EF-G·GTP (3 μM) and Pmn (10 mM) and translocation analysed by formation of <t>fMetPhe-Pmn.</t> The amount of pre-translocation complex (PTC) was determined by <t>HPLC</t> analysis of fMetPhe. B. Translocation was monitored by the fluorescence change of fMetPhe-tRNA Phe (Prf16/17). Curve 1 – control ribosomes; curve 2 – colicin E3-cleaved ribosomes; curve 3 – control ribosomes in the presence of viomycin (200 μM); curve 4 – colicin E3-cleaved ribosomes with viomycin (200 μM). Normalized ΔF, fluorescence change normalized by the maximum extent of translocation determined by the Pmn reaction. C. Pi release upon GTP hydrolysis by EF-G (curves 1 and 2) or buffer control (curves 3 and 4) with control ribosomes (curves 1 and 3) or colicin E3-cleaved (curves 2 and 4). Pi release was measured by the fluorescence change of MDCC-PBP upon Pi binding ( Experimental procedures ). D. Multiple-turnover GTP hydrolysis by EF-G. Velocity of GTP hydrolysis was measured with catalytic concentrations of EF-G (10 nM) and increasing concentrations of colicin E3-cleaved ribosomes (closed circles) or control ribosomes (open circles) in the presence of excess [γ- 32 P]-GTP (200 μM).
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1) Product Images from "Colicin E3 cleavage of 16S rRNA impairs decoding and accelerates tRNA translocation on Escherichia coli ribosomes"

Article Title: Colicin E3 cleavage of 16S rRNA impairs decoding and accelerates tRNA translocation on Escherichia coli ribosomes

Journal: Molecular Microbiology

doi: 10.1111/j.1365-2958.2008.06283.x

Translocation. A. Colicin E3-cleaved (closed circles) or control (open circles) pre-translocation complexes (0.1 μM) were mixed in a quench-flow apparatus with EF-G·GTP (3 μM) and Pmn (10 mM) and translocation analysed by formation of fMetPhe-Pmn. The amount of pre-translocation complex (PTC) was determined by HPLC analysis of fMetPhe. B. Translocation was monitored by the fluorescence change of fMetPhe-tRNA Phe (Prf16/17). Curve 1 – control ribosomes; curve 2 – colicin E3-cleaved ribosomes; curve 3 – control ribosomes in the presence of viomycin (200 μM); curve 4 – colicin E3-cleaved ribosomes with viomycin (200 μM). Normalized ΔF, fluorescence change normalized by the maximum extent of translocation determined by the Pmn reaction. C. Pi release upon GTP hydrolysis by EF-G (curves 1 and 2) or buffer control (curves 3 and 4) with control ribosomes (curves 1 and 3) or colicin E3-cleaved (curves 2 and 4). Pi release was measured by the fluorescence change of MDCC-PBP upon Pi binding ( Experimental procedures ). D. Multiple-turnover GTP hydrolysis by EF-G. Velocity of GTP hydrolysis was measured with catalytic concentrations of EF-G (10 nM) and increasing concentrations of colicin E3-cleaved ribosomes (closed circles) or control ribosomes (open circles) in the presence of excess [γ- 32 P]-GTP (200 μM).
Figure Legend Snippet: Translocation. A. Colicin E3-cleaved (closed circles) or control (open circles) pre-translocation complexes (0.1 μM) were mixed in a quench-flow apparatus with EF-G·GTP (3 μM) and Pmn (10 mM) and translocation analysed by formation of fMetPhe-Pmn. The amount of pre-translocation complex (PTC) was determined by HPLC analysis of fMetPhe. B. Translocation was monitored by the fluorescence change of fMetPhe-tRNA Phe (Prf16/17). Curve 1 – control ribosomes; curve 2 – colicin E3-cleaved ribosomes; curve 3 – control ribosomes in the presence of viomycin (200 μM); curve 4 – colicin E3-cleaved ribosomes with viomycin (200 μM). Normalized ΔF, fluorescence change normalized by the maximum extent of translocation determined by the Pmn reaction. C. Pi release upon GTP hydrolysis by EF-G (curves 1 and 2) or buffer control (curves 3 and 4) with control ribosomes (curves 1 and 3) or colicin E3-cleaved (curves 2 and 4). Pi release was measured by the fluorescence change of MDCC-PBP upon Pi binding ( Experimental procedures ). D. Multiple-turnover GTP hydrolysis by EF-G. Velocity of GTP hydrolysis was measured with catalytic concentrations of EF-G (10 nM) and increasing concentrations of colicin E3-cleaved ribosomes (closed circles) or control ribosomes (open circles) in the presence of excess [γ- 32 P]-GTP (200 μM).

Techniques Used: Translocation Assay, Flow Cytometry, High Performance Liquid Chromatography, Fluorescence, Binding Assay

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High Performance Liquid Chromatography:

Article Title: Colicin E3 cleavage of 16S rRNA impairs decoding and accelerates tRNA translocation on Escherichia coli ribosomes
Article Snippet: .. The amount of fMetPhe formed was determined by reversed-phase HPLC (Lichrospher 100 RP-8, Merck). .. The rate of translocation was determined by the reaction of translocated peptidyl-tRNA with Pmn, as monitored by quench-flow ( ).

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Chromatography:

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Labeling:

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Incubation:

Article Title: A common SNP in ER aminopeptidase 2 induces a specificity switch that leads to altered antigen processing
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Thin Layer Chromatography:

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    DFT1+IFNγ and DFT2 cell lines have a restricted repertoire of <t>MHC</t> class I (MHC-I) alleles compared to devil fibroblasts. (a) Table of devil MHC-I alleles identified in at least three out of four replicates in devil cell lines by analysis of the heavy chain (HC) fraction separated by <t>HPLC</t> in this paper (shaded boxes) or by mRNA analysis (crossed boxes) in a previous publication ( 1 ). A devil fibroblast cell line (referred to as Fibroblasts) represents a host devil. DFT1 is represented by the cell line 4906 treated with interferon γ to induce MHC-I expression (DFT1+IFNγ in the table text) and DFT2 is represented by the cell line Red Velvet (DFT2 in the table text). (b) Quantification of HCs of MHC-I alleles in (a) represented as normalised intensity. Statistically significant comparison (p
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    DFT1+IFNγ and DFT2 cell lines have a restricted repertoire of MHC class I (MHC-I) alleles compared to devil fibroblasts. (a) Table of devil MHC-I alleles identified in at least three out of four replicates in devil cell lines by analysis of the heavy chain (HC) fraction separated by HPLC in this paper (shaded boxes) or by mRNA analysis (crossed boxes) in a previous publication ( 1 ). A devil fibroblast cell line (referred to as Fibroblasts) represents a host devil. DFT1 is represented by the cell line 4906 treated with interferon γ to induce MHC-I expression (DFT1+IFNγ in the table text) and DFT2 is represented by the cell line Red Velvet (DFT2 in the table text). (b) Quantification of HCs of MHC-I alleles in (a) represented as normalised intensity. Statistically significant comparison (p

    Journal: bioRxiv

    Article Title: Passage of transmissible cancers in the Tasmanian devil is due to a dominant, shared peptide motif and a limited repertoire of MHC-I allotypes

    doi: 10.1101/2020.07.03.184416

    Figure Lengend Snippet: DFT1+IFNγ and DFT2 cell lines have a restricted repertoire of MHC class I (MHC-I) alleles compared to devil fibroblasts. (a) Table of devil MHC-I alleles identified in at least three out of four replicates in devil cell lines by analysis of the heavy chain (HC) fraction separated by HPLC in this paper (shaded boxes) or by mRNA analysis (crossed boxes) in a previous publication ( 1 ). A devil fibroblast cell line (referred to as Fibroblasts) represents a host devil. DFT1 is represented by the cell line 4906 treated with interferon γ to induce MHC-I expression (DFT1+IFNγ in the table text) and DFT2 is represented by the cell line Red Velvet (DFT2 in the table text). (b) Quantification of HCs of MHC-I alleles in (a) represented as normalised intensity. Statistically significant comparison (p

    Article Snippet: Separation of MHC-I eluate by RP-HPLC : eluted peptides were separated from MHC-I heavy chains, β2m and other contaminants using a C18 reversed-phase HPLC column (4.6 mm internal diameter x 10 cm, Chromolith Speed Rod, Merck) running on a mobile phase buffer of buffer A (0.1% trifluoroacetic acid (TFA)) and buffer B (80% acetonitrile/0.1% TFA) on an AKTAmicro™ HPLC system (GE Healthcare).

    Techniques: High Performance Liquid Chromatography, Expressing

    Translocation. A. Colicin E3-cleaved (closed circles) or control (open circles) pre-translocation complexes (0.1 μM) were mixed in a quench-flow apparatus with EF-G·GTP (3 μM) and Pmn (10 mM) and translocation analysed by formation of fMetPhe-Pmn. The amount of pre-translocation complex (PTC) was determined by HPLC analysis of fMetPhe. B. Translocation was monitored by the fluorescence change of fMetPhe-tRNA Phe (Prf16/17). Curve 1 – control ribosomes; curve 2 – colicin E3-cleaved ribosomes; curve 3 – control ribosomes in the presence of viomycin (200 μM); curve 4 – colicin E3-cleaved ribosomes with viomycin (200 μM). Normalized ΔF, fluorescence change normalized by the maximum extent of translocation determined by the Pmn reaction. C. Pi release upon GTP hydrolysis by EF-G (curves 1 and 2) or buffer control (curves 3 and 4) with control ribosomes (curves 1 and 3) or colicin E3-cleaved (curves 2 and 4). Pi release was measured by the fluorescence change of MDCC-PBP upon Pi binding ( Experimental procedures ). D. Multiple-turnover GTP hydrolysis by EF-G. Velocity of GTP hydrolysis was measured with catalytic concentrations of EF-G (10 nM) and increasing concentrations of colicin E3-cleaved ribosomes (closed circles) or control ribosomes (open circles) in the presence of excess [γ- 32 P]-GTP (200 μM).

    Journal: Molecular Microbiology

    Article Title: Colicin E3 cleavage of 16S rRNA impairs decoding and accelerates tRNA translocation on Escherichia coli ribosomes

    doi: 10.1111/j.1365-2958.2008.06283.x

    Figure Lengend Snippet: Translocation. A. Colicin E3-cleaved (closed circles) or control (open circles) pre-translocation complexes (0.1 μM) were mixed in a quench-flow apparatus with EF-G·GTP (3 μM) and Pmn (10 mM) and translocation analysed by formation of fMetPhe-Pmn. The amount of pre-translocation complex (PTC) was determined by HPLC analysis of fMetPhe. B. Translocation was monitored by the fluorescence change of fMetPhe-tRNA Phe (Prf16/17). Curve 1 – control ribosomes; curve 2 – colicin E3-cleaved ribosomes; curve 3 – control ribosomes in the presence of viomycin (200 μM); curve 4 – colicin E3-cleaved ribosomes with viomycin (200 μM). Normalized ΔF, fluorescence change normalized by the maximum extent of translocation determined by the Pmn reaction. C. Pi release upon GTP hydrolysis by EF-G (curves 1 and 2) or buffer control (curves 3 and 4) with control ribosomes (curves 1 and 3) or colicin E3-cleaved (curves 2 and 4). Pi release was measured by the fluorescence change of MDCC-PBP upon Pi binding ( Experimental procedures ). D. Multiple-turnover GTP hydrolysis by EF-G. Velocity of GTP hydrolysis was measured with catalytic concentrations of EF-G (10 nM) and increasing concentrations of colicin E3-cleaved ribosomes (closed circles) or control ribosomes (open circles) in the presence of excess [γ- 32 P]-GTP (200 μM).

    Article Snippet: The amount of fMetPhe formed was determined by reversed-phase HPLC (Lichrospher 100 RP-8, Merck).

    Techniques: Translocation Assay, Flow Cytometry, High Performance Liquid Chromatography, Fluorescence, Binding Assay

    Panel A, specificity index (defined as the trimming rate for a peptide with a positively charged N-terminus divided by the trimming rate for the same peptide carrying a hydrophobic N-terminus) for three different antigenic epitope templates using the two ERAP2 variants. Y-axis is broken to enhance visibility of large numerical differences. Panel B , RP-HPLC chromatograms of trimming of the precursor RSRYWAIRTR by ERAP2 N and ERAP2 K . Notice the similar amount of epitope generation. Panel C, RP-HPLC chromatograms of trimming of the precursor LSRYWAIRTR by ERAP2 N and ERAP2 K . Notice the absence of a visible epitope peak produced by ERAP2 K .

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: A common SNP in ER aminopeptidase 2 induces a specificity switch that leads to altered antigen processing

    doi: 10.4049/jimmunol.1200918

    Figure Lengend Snippet: Panel A, specificity index (defined as the trimming rate for a peptide with a positively charged N-terminus divided by the trimming rate for the same peptide carrying a hydrophobic N-terminus) for three different antigenic epitope templates using the two ERAP2 variants. Y-axis is broken to enhance visibility of large numerical differences. Panel B , RP-HPLC chromatograms of trimming of the precursor RSRYWAIRTR by ERAP2 N and ERAP2 K . Notice the similar amount of epitope generation. Panel C, RP-HPLC chromatograms of trimming of the precursor LSRYWAIRTR by ERAP2 N and ERAP2 K . Notice the absence of a visible epitope peak produced by ERAP2 K .

    Article Snippet: Analysis of digestion products after incubation of peptides with ERAP1 or ERAP2 was performed by RP-HPLC on a Chromolith C-18 analytical column (Merck) as previously described ( ).

    Techniques: High Performance Liquid Chromatography, Produced

    Panel A, RP-HPLC chromatograms of products of the enzymatic digestion of peptide LSRHHAFSFR (substrate) by the two ERAP2 variants. The produced epitope SRHHAFSFR (product) is indicated. Two characteristic reaction conditions are shown, using 200ng (14.7nM, molar ratio peptide to enzyme=1361) of enzyme for 15min or 1hr and 2μg (147nM, molar ratio peptide to enzyme=136) enzyme for 1hr. Panel B, epitope generation rate for each ERAP2 variant. Panel C ). Panel D , turnover number (k cat ) and specificity constant (k cat /K M ) for the production of the SRHHAFSFR epitope by the two ERAP2 variants.

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: A common SNP in ER aminopeptidase 2 induces a specificity switch that leads to altered antigen processing

    doi: 10.4049/jimmunol.1200918

    Figure Lengend Snippet: Panel A, RP-HPLC chromatograms of products of the enzymatic digestion of peptide LSRHHAFSFR (substrate) by the two ERAP2 variants. The produced epitope SRHHAFSFR (product) is indicated. Two characteristic reaction conditions are shown, using 200ng (14.7nM, molar ratio peptide to enzyme=1361) of enzyme for 15min or 1hr and 2μg (147nM, molar ratio peptide to enzyme=136) enzyme for 1hr. Panel B, epitope generation rate for each ERAP2 variant. Panel C ). Panel D , turnover number (k cat ) and specificity constant (k cat /K M ) for the production of the SRHHAFSFR epitope by the two ERAP2 variants.

    Article Snippet: Analysis of digestion products after incubation of peptides with ERAP1 or ERAP2 was performed by RP-HPLC on a Chromolith C-18 analytical column (Merck) as previously described ( ).

    Techniques: High Performance Liquid Chromatography, Produced, Variant Assay

    Reverse phase HPLC of radiolabeled ligand. (a) 99m Tc-tricine-ligand in multiwavelength detector (λ = 280 nm) and (b) for radiocomplex in Raytest-Gabi gamma-detector. CC 250/4.6 Nucleosil 120-5 C-18 column from Teknokroma was used. 0.1% trifluoroacetic acid/water (Solvent A) and 0.1% trifluoroacetic acid/acetonitrile (Solvent B) were used as a mobile phase in the following gradient: 0 min 95% A (5% B), 5 min 95% A (5% B), 25 min 0% A (100% B), 30 min 0% A (100% B), flow = 1 mL/min

    Journal: Iranian Journal of Pharmaceutical Research : IJPR

    Article Title: Evaluation of a 99mTc-tricine Vascular Disrupting Agent as an In-vivo Imaging in 4T1 Mouse Breast Tumor Model

    doi:

    Figure Lengend Snippet: Reverse phase HPLC of radiolabeled ligand. (a) 99m Tc-tricine-ligand in multiwavelength detector (λ = 280 nm) and (b) for radiocomplex in Raytest-Gabi gamma-detector. CC 250/4.6 Nucleosil 120-5 C-18 column from Teknokroma was used. 0.1% trifluoroacetic acid/water (Solvent A) and 0.1% trifluoroacetic acid/acetonitrile (Solvent B) were used as a mobile phase in the following gradient: 0 min 95% A (5% B), 5 min 95% A (5% B), 25 min 0% A (100% B), 30 min 0% A (100% B), flow = 1 mL/min

    Article Snippet: Labeling analysis and stability 99m Tc-tricine-ligand was characterized by analytical RP-HPLC and TLC on silica gel 60 (Merck) using different mobile phases: 2-butanone for free 99m TcO4 - (Rf = 1), and water/acetonitrile 1/1 for 99m Tc colloid (Rf = 0).

    Techniques: High Performance Liquid Chromatography, Flow Cytometry